Authors

Document Type

Degree

Major/Program

First Advisor's Name

First Advisor's Committee Title

Committee Chair

Second Advisor's Name

Kathleen Rein

Third Advisor's Name

Watson Lees

Keywords

HPLC, Enantioseparation, Chloroperoxidase, Dimethylsulfoniopropionate

Date of Defense

11-10-2011

Abstract

Chloroperoxidase (CPO), secreted by marine fungus Caldariomycesfumago, is the most versatile catalyst among known heme enzymes. Chloroperoxidase can catalyze epoxidation reactions with high enantioselectivity and high yield, which makes CPO an attractive candidate for both industrial and medicinal chiral synthesis. Toward this end, we have constructed two CPO mutants, F103A and N74V. Chiral HPLC was used to evaluate the enantioselectivity and yield of CPO and the mutants toward the epoxidation of styrene and its derivatives. Both of the mutants show dramatically changed epoxidation profiles compared to the parent protein. This information provided fresh insight into the mechanism through which CPO achieves its enantioselectivity. Furthermore, effort was made to understand the biological function of CPO through characterization of CPO catalyzed oxidation of dimethylsulfoniopropionate (DMSP), a secondary metabolite of many marine algal species that plays a pivotal role in marine ecology and global climate.

Downloads

Share

DOI

Rights Statement

In Copyright. URI: http://rightsstatements.org/vocab/InC/1.0/This Item is protected by copyright and/or related rights. You are free to use this Item in any way that is permitted by the copyright and related rights legislation that applies to your use. For other uses you need to obtain permission from the rights-holder(s).